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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sillence, M. N. Pegg, G. G. Moore, N. G. Lindsay, D. B. |
| Description | Author Affiliation: Sillence MN ( CSIRO Division of Tropical Animal Production, University of Central Queensland, Rockhampton, Australia.) |
| Abstract | 1. The beta-adrenoceptor population was characterized in membrane preparations from rat brown adipose tissue (BAT) and from soleus muscle by use of the radioligand [125I]-iodocyanopindolol ([125I]-ICYP). In addition, atypical binding sites for [125I]-ICYP found in both tissues were examined, and the relationship between these sites and the putative rat beta 3-adrenoceptor is discussed. 2. It was established that BAT membranes host a mixed population of beta 1- and beta 2-adrenoceptors. Of these two sites, 55% showed a high affinity for the beta 1-selective ligand CGP 20712A (pK 8.5), and 45% showed a high affinity for the beta 2-selective antagonist ICI 118551 (pK 8.6). Soleus muscle membranes were found to host a population of beta 2-adrenoceptors, characterized by a high affinity for ICI 118551 (pK 9.1), but beta 1-adrenoceptors could not be detected in this preparation. 5-Hydroxytryptamine receptors were not detected in either preparation. 3. In addition to beta 1- and beta 2-adrenoceptors, atypical binding sites were identified in both tissues using high concentrations of radioligand (0.5-0.6 nM) and in the presence of 1 microM (-)-propranolol. The atypical sites were abundant, representing 80 and 81% of the total [125I]-ICYP binding sites in BAT and soleus muscle respectively. When the pK values for 11 ligands were compared, the correlation coefficient for atypical sites in BAT and soleus muscle was 0.94. 4. The atypical binding sites showed a moderate affinity for (+/-)-cyanopindolol (pK 7.3-7.7), poor stereo selectivity for the (+)- and (-)-enantiomers of alprenolol (<10 fold), and a low affinity for B-adrenoceptor antagonists and partial agonists in the order: (+/-)-cyanopindolol>(-)-alprenolol>(-)-propranolol=(+/-)-ICI 118551>>(+/-)-CGP20712A. The affinity of these ligands for the atypical sites reflects their behaviour in functional studies of putative beta 3-adrenoceptors in rat BAT, white adipose tissue, intestine and colon.5. The atypical sites labelled by [125I]-ICYP were resistant to agonist binding, and while the order of affinity of the agonists BRL 37344> isoprenaline> noradrenaline matches their order of potency at putative beta 3-adrenoceptors, none of these compounds caused displacement of the radioligand at concentrations below 10 microM.6. It is concluded that the atypical binding sites for [125I]-ICYP found in rat BAT and soleus muscle membranes are the same, and that these sites show some relationship to the putative rat beta 3-adrenoceptor identified in functional studies using antagonists. However, under the conditions used in the present study, pK values obtained for beta 3-agonist binding are not useful. |
| ISSN | 00071188 |
| e-ISSN | 14765381 |
| Journal | British Journal of Pharmacology |
| Issue Number | 4 |
| Volume Number | 109 |
| Language | English |
| Publisher | Wiley Online Library(on behalf of The British Pharmacological Society) |
| Publisher Date | 1993-08-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Adipose Tissue, Brown Metabolism Muscles Receptors, Adrenergic, Beta Adrenergic Beta-Agonists Adrenergic Beta-Antagonists Animals Cell Membrane In Vitro Techniques Iodine Radioisotopes Iodocyanopindolol Ligands Pindolol Analogs & Derivatives Radioligand Assay Rats, Wistar Comparative Study Research Support, Non-U.S. Gov't Pharmacology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Pharmacology |
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